Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.214 - tRNA (guanine10-N2)-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q12463

for references in articles please use BRENDA:EC2.1.1.214
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.214 tRNA (guanine10-N2)-methyltransferase
IUBMB Comments
In contrast to the archaeal enzyme tRNA (guanine10-N2)-dimethyltransferase (EC 2.1.1.213), tRNA (guanine10-N2)-methyltransferase from yeast does not catalyse the methylation from N2-methylguanine10 to N2-dimethylguanine10 in tRNA.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q12463
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
hide
S-adenosyl-L-methionine
+
guanine10 in tRNA
=
S-adenosyl-L-homocysteine
+
N2-methylguanine10 in tRNA
+
guanine10 in tRNA
=
+
N2-methylguanine10 in tRNA
Synonyms
trm11, trna mtase, archaeal trm11, trm11p, trm11-trm112 complex, yol124c, eukaryotic trm11, n2,n2-dimethylguanosine trna methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(m2G10) methyltransferase
-
eukaryotic m2G10 tRNA methyltransferase
-
Trm11-Trm112 complex
-
Trm11p
catalytic subunit
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine10-N2)-methyltransferase
In contrast to the archaeal enzyme tRNA (guanine10-N2)-dimethyltransferase (EC 2.1.1.213), tRNA (guanine10-N2)-methyltransferase from yeast does not catalyse the methylation from N2-methylguanine10 to N2-dimethylguanine10 in tRNA.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine10 in tRNAIle(AAU)
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNAIle(AAU)
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
the enzyme is composed of at least two subunits that are associated in vivo: Trm11p, which is the catalytic subunit, and Trm112p, a putative zinc-binding protein
Zn2+
zinc might be important for Trm11 binding to Trm112, most probably by maintaining the three-dimensional structure of Trm112 zinc-binding domain, which in the other Trm112-MTase complexes is directly interacting with the MTase domains
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Zinc
the regulatory subunit Trm112 contains a zinc-finger
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TRM112
dependent on, Trm11 proves to be completely inactive alone. This lack of activity cannot be attributed to protein unfolding as the circular dichroism (CD) spectrum recorded on this protein is typical of well-folded proteins containing alpha-helices and beta-strands. Trm112 stimulates SAM binding to Trm11 and contributes to tRNA binding. Analysis of the activation mode of the eukaryotic m2G10 tRNA methyltransferase Trm11 by its partner protein Trm112. Yeast Trm112 has a calculated molecular weight of 15067.6 Da. A zinc atom is attached to its Zn-binding domain. The Trm112-Trm11 interaction mode is reminiscent of the other Trm112-MTase complexes. Three-dimensional Trm11-Trm112 complex structrue analysis, and thermodynamics of interaction at 10°C, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten steady-state kinetics analysis
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
While deletion of TRM11 has no detectable phenotype under laboratory conditions, deletion of TRM112 leads to a severe growth defect, suggesting that it has additional functions in the cell
physiological function
the enzyme is active only in complex with its partner protein Trm112, Trm11 proves to be completely inactive alone. The Trm112-Trm11 interaction mode is reminiscent of the other Trm112-MTase complexes. zinc might be important for Trm11 binding to Trm112, most probably by maintaining the three-dimensional structure of Trm112 zinc-binding domain, which in the other Trm112-MTase complexes is directly interacting with the MTase domains. Trm112 stimulates SAM binding to Trm11 and contributes to tRNA binding. Also the tRNA 3'-CCA tail from the aminoacyl stem loop for tRNA is important for methyltransferase activity
malfunction
-
TRM112 mutant strains show growth defects, as well as nuclear genomic instability and mitotic defects, overview. Chromosome instability increases 6-7-fold in trm112-0 compared with wild-type. trm112-0 strain is resistant to zymocin, thetRNase toxin produced by Kluyveromyces lactis that specifically targets the mcm5s2U modification at position 34 and cleaves tRNAUUGGln, tRNAUUCGlu, and tRNAUUU
physiological function
-
Trm11p and Trm112p are two interacting proteins that are both required for catalyzing the formation of m2G at position 10 in several tRNAs. Trm11p is the catalytic subunit, but also Trm112p is essential for the formation of m2G10, Trm112p is essential for the activity of Trm11p, another tRNA methyltransferase, because Trm112p is capable of directing the proper folding of Trm11p, leading to the synthesis of an active complex. Trm112p is required in vivo for the formation of mcm5U34 and mcm5s2U34, overview. Trm112p is also required for the activity of Mtq2p, a protein methyltransferase that catalyzes the methylation of the glutamine of the universally conserved GGQ tripeptide of the translation termination factor eRF1/Sup45. Trm112p is associated with other partners involved in ribosome biogenesis and chromatin remodeling, suggesting that it has additional roles in the cell
additional information
generation of a Saccharomyces cerevisiae Trm11-Trm112 three-dimensional structure model, overview, the Trm11 region encompasses residues 1 to 406
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66322
a heterodimeric Trm11-Trm112 complex in the presence of zinc, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 51109, His-tagged enzyme, sequence calculation
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
a plasmid containing a wild-type copy of the TRM112 gene (pBL652) is able to restore the formation of the two modified nucleosides in a trm112-0 strain
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble C-terminally His6-tagged wild-type and mutant enzymes to homogeneity from Escherichia coli strain BL21-Gold (DE3) by nickel affinity chromatography and gel filtration
recombinant His-tagged Trm112p, alone or with Trm9p, from Escherichia coli strain S15 (DE3-pLysS) by nickel affinity chromatography and desalting gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene YOL124c, recombinant expression of soluble C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Gold (DE3), coexpression of yeast Trm11 with yeast Trm112 in Escherichia coli, the holonezyme complex is active
recombinant Trm11p expressed in Escherichia coli exhibited no m2G10 formation activity. Trm112p and Trm11p are both required for the formation of m2G10 in vivo as well as in vitro
gene TRM112, phylogenetic analysis, expression of His-tagged Trm112p, alone or with Trm9p, in Escherichia coli strain S15 (DE3-pLysS), Trm112p forms a complex with Trm9p, which renders the latter soluble
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Purushothaman, S.K.; Bujnicki, J.M.; Grosjean, H.; Lapeyre, B.
Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA
Mol. Cell. Biol.
25
4359-4370
2005
Saccharomyces cerevisiae (Q12463), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Okada, K.; Muneyoshi, Y.; Endo, Y.; Hori, H.
Production of yeast (m2G10) methyltransferase (Trm11 and Trm112 complex) in a wheat germ cell-free translation system
Nucleic Acids Symp. Ser.
53
303-304
2009
Saccharomyces cerevisiae (Q12463), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mazauric, M.H.; Dirick, L.; Purushothaman, S.K.; Bjrk, G.R.; Lapeyre, B.
Trm112p is a 15-kDa zinc finger protein essential for the activity of two tRNA and one protein methyltransferases in yeast
J. Biol. Chem.
285
18505-18515
2010
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Bourgeois, G.; Marcoux, J.; Saliou, J.M.; Cianferani, S.; Graille, M.
Activation mode of the eukaryotic m2G10 tRNA methyltransferase Trm11 by its partner protein Trm112
Nucleic Acids Res.
45
1971-1982
2017
Saccharomyces cerevisiae (Q12463), Saccharomyces cerevisiae ATCC 204508 (Q12463)
Manually annotated by BRENDA team